CRCU

Chemical Research in Chinese Universities ›› 2004, Vol. 20 ›› Issue (1): 55-59.

• Articles • Previous Articles     Next Articles

Construction of Hybrid Enzyme from HEC-SOD and Cu,Zn-SOD

GOU Xiao-jun1, ZHANG Zhong-hua2, LI Shuang2, KONG Xiang-duo2, SUN Yan-hong2, LIU Wei1, ZHAGN Jin2   

  1. 1. The Joint Laboratory of Molecular Evolution and Engineering, Department of Bioengineering, Chengdu University, Chengdu 610106, P. R. China;
    2. Key Lab for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun 130023, P. R. China
  • Received:2003-01-09 Online:2004-02-24 Published:2011-08-06

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Abstract: Human extracellular superoxide dismutase(hEC-SOD) is a secreted tetrameric protein involved in the protection of a human body from oxygen free radicals. Its three-dimensional structure has not been confirmed. hEC-SOD couldn′t be expressed in E.coli. We constructed a hybrid enzyme, which comprises the N-terminal and C-terminal domains from hEC-SOD, fused it to human Cu,Zn-SOD. The hybrid enzyme is expressed successfully in E.coli. Further, we analyzed the expression of hEC-SOD in E.coli by mRNA differential displaying.

Key words: Extracellular superoxide dismutase, Hybrid enzyme, mRNA differential displaying